Effect of sucrose on the thermodynamic incompatibility of different biopolymers

Modulation of the thermodynamic stability of proteins by polyols: Significance of polyol hydrophobicity and impact on the chemical potential of water

“…Several polyols including sucrose have been observed to increase the solubility of proteins in solution (Antipova and Semenova, 1996;Conti et al, 1997;Farnum and Zukoski, 1999), an observation which theoretically counteracts exclusion. Since polyols increase the chemical potential of the protein molecules, it is anticipated that preferentially excluded co-solvents will favor the solid state over the dissolved state as this would minimize the area of the protein molecules that is exposed to the co-solvent environment.…”

Volumetric, viscometric, and refractive index behaviour of α-amino acids and their groups’ contribution in aqueous d-glucose solution at different temperatures

“…It is widely recognised that sugars (as cosolutes) help in stabilizing biological macromolecules [19]. This action is performed either due to direct interactions between them and/or through alteration of the water structure [20][21][22]. These considerations led us to undertake the study of amino acids (glycine 0021 (Gly), DL-alanine (Ala), L-serine (Ser), and DL-valine (Val)) in concentration range (0.1 to 0.5) M in 0.2 M aqueous D-glucose solution at different temperatures.…”

The effects of sucrose on the mechanical properties of acid milk proteins-kappa-carrageenan gels

“…Sugar changes qualitatively the structural and rheological properties, strengthening caseincasein and casein-polysaccharide interactions . Previous studies have shown that low-molecular-weight sugars, and particularly sucrose, can cause various marked changes in functional properties of casein: (i) an increase in the solubility of sodium caseinate in aqueous medium in the vicinity of the isoelectric point of the protein (Antipova and Semenova, 1995); (ii) an increase in the thermodynamic compatibility of casein with polysaccharides in bulk aqueous media (Antipova and Semenova, 1995;Schorsch et al, 1999); (iii) an increase in the surface activity of sodium caseinate at the planar air-water interface (Antipova et al, 1999); (iv) a substantial increase in the acid-induced gel-forming ability of sodium caseinate and (v) a marked enhancement of the viscoelasticity of acidinduced casein gels due to the effects of sucrose on the self-association of sodium caseinate (Belyakova et al, 2003).…”